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Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)
| Field | Value |
|---|---|
| Name | Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) |
| EC_number | 2.5.1.87 |
Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) (, RER2, Rer2p, Rer2p Z-prenyltransferase, Srt1p, Srt2p Z-prenyltransferase, ACPT, dehydrodolichyl diphosphate synthase 1) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10--55 isopentenyl units). This enzyme catalyses the following chemical reaction
: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate \rightleftharpoons n diphosphate + ditrans, polycis-polyprenyl diphosphate (n \rightleftharpoons 10--55)
The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit.
References
References
- (June 2001). "Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis". Genes to Cells.
- (June 2007). "Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae". Biopolymers.
- (January 1999). "The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis". Molecular and Cellular Biology.
- (June 2000). "Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis". The Journal of Biological Chemistry.
- (July 2000). "Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis". FEBS Letters.
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